Purification and properties of an acidic β-glucosidase from Acidobacterium capsulatum

Noriaki Kishimoto, Kenji Inagaki, Tsuyoshi Sugio, Tatsuo Tano

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Acidobacterium capsulatum, an acidophilic, mesophilic and chemoorganotrophic bacterium, produced an inducible, acidic β-glucosidase in the cellobiose medium. The enzyme was successively purified 109 times by CM-Sepharose, Sephacryl S-200 chromatography and preparative discontinuous polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis of the purified enzyme gave a single band at pH 4.3. The enzyme had an optimum pH of 3.0 and optimum reaction temperature of 55°C, being stable from pH 1.5 to 6.0 and at temperatures from 20 to 45°C. No activity was detected above pH 6.5 or above 65°C. The molecular weight of 90,000 was estimated by gel filtration and the enzyme had an isoelectric point of 7.0. The enzyme hydrolyzed aryl-β-glycosides and β-linked disaccharides.

Original languageEnglish
Pages (from-to)318-321
Number of pages4
JournalJournal of Fermentation and Bioengineering
Volume71
Issue number5
DOIs
Publication statusPublished - 1991

Fingerprint

Acidobacteria
Glucosidases
Purification
Enzymes
Gels
Polyacrylates
Electrophoresis
Polyacrylamide Gel Electrophoresis
Glycosides
Cellobiose
Temperature
Disaccharides
Isoelectric Point
Chromatography
Sepharose
Gel Chromatography
Bacteria
Molecular Weight
Molecular weight

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Purification and properties of an acidic β-glucosidase from Acidobacterium capsulatum. / Kishimoto, Noriaki; Inagaki, Kenji; Sugio, Tsuyoshi; Tano, Tatsuo.

In: Journal of Fermentation and Bioengineering, Vol. 71, No. 5, 1991, p. 318-321.

Research output: Contribution to journalArticle

Kishimoto, Noriaki ; Inagaki, Kenji ; Sugio, Tsuyoshi ; Tano, Tatsuo. / Purification and properties of an acidic β-glucosidase from Acidobacterium capsulatum. In: Journal of Fermentation and Bioengineering. 1991 ; Vol. 71, No. 5. pp. 318-321.
@article{fb5eb3f7ebc84439bae6ed9133ea9e1e,
title = "Purification and properties of an acidic β-glucosidase from Acidobacterium capsulatum",
abstract = "Acidobacterium capsulatum, an acidophilic, mesophilic and chemoorganotrophic bacterium, produced an inducible, acidic β-glucosidase in the cellobiose medium. The enzyme was successively purified 109 times by CM-Sepharose, Sephacryl S-200 chromatography and preparative discontinuous polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis of the purified enzyme gave a single band at pH 4.3. The enzyme had an optimum pH of 3.0 and optimum reaction temperature of 55°C, being stable from pH 1.5 to 6.0 and at temperatures from 20 to 45°C. No activity was detected above pH 6.5 or above 65°C. The molecular weight of 90,000 was estimated by gel filtration and the enzyme had an isoelectric point of 7.0. The enzyme hydrolyzed aryl-β-glycosides and β-linked disaccharides.",
author = "Noriaki Kishimoto and Kenji Inagaki and Tsuyoshi Sugio and Tatsuo Tano",
year = "1991",
doi = "10.1016/0922-338X(91)90343-F",
language = "English",
volume = "71",
pages = "318--321",
journal = "Journal of Bioscience and Bioengineering",
issn = "1389-1723",
publisher = "The Society for Biotechnology, Japan",
number = "5",

}

TY - JOUR

T1 - Purification and properties of an acidic β-glucosidase from Acidobacterium capsulatum

AU - Kishimoto, Noriaki

AU - Inagaki, Kenji

AU - Sugio, Tsuyoshi

AU - Tano, Tatsuo

PY - 1991

Y1 - 1991

N2 - Acidobacterium capsulatum, an acidophilic, mesophilic and chemoorganotrophic bacterium, produced an inducible, acidic β-glucosidase in the cellobiose medium. The enzyme was successively purified 109 times by CM-Sepharose, Sephacryl S-200 chromatography and preparative discontinuous polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis of the purified enzyme gave a single band at pH 4.3. The enzyme had an optimum pH of 3.0 and optimum reaction temperature of 55°C, being stable from pH 1.5 to 6.0 and at temperatures from 20 to 45°C. No activity was detected above pH 6.5 or above 65°C. The molecular weight of 90,000 was estimated by gel filtration and the enzyme had an isoelectric point of 7.0. The enzyme hydrolyzed aryl-β-glycosides and β-linked disaccharides.

AB - Acidobacterium capsulatum, an acidophilic, mesophilic and chemoorganotrophic bacterium, produced an inducible, acidic β-glucosidase in the cellobiose medium. The enzyme was successively purified 109 times by CM-Sepharose, Sephacryl S-200 chromatography and preparative discontinuous polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis of the purified enzyme gave a single band at pH 4.3. The enzyme had an optimum pH of 3.0 and optimum reaction temperature of 55°C, being stable from pH 1.5 to 6.0 and at temperatures from 20 to 45°C. No activity was detected above pH 6.5 or above 65°C. The molecular weight of 90,000 was estimated by gel filtration and the enzyme had an isoelectric point of 7.0. The enzyme hydrolyzed aryl-β-glycosides and β-linked disaccharides.

UR - http://www.scopus.com/inward/record.url?scp=0025769164&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025769164&partnerID=8YFLogxK

U2 - 10.1016/0922-338X(91)90343-F

DO - 10.1016/0922-338X(91)90343-F

M3 - Article

AN - SCOPUS:0025769164

VL - 71

SP - 318

EP - 321

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

SN - 1389-1723

IS - 5

ER -